| Authors: |
Christine EBEL, Cécile Breyton, Annelise Vermot, Franck Fieschi, Wakas Javed, Jean-Michel Jault, Cédric Orelle, Anne Martel
|
|---|
| Abstract: |
Small Angle Neutron Scattering (SANS) is a low-resolution technique enable to probe the solution structure of individual biomacromolecules complexed with partners. In particular, concerning membrane proteins, the membrane-like environment can be made invisible in order to see only the protein (Ebel et al, Methods Mol Biol. 2020). Membrane proteins are often not extremely stable in detergent solutions We showed that the detergent LMNG is good detergent preserving membrane proteins stability and homogeneity (Breyton et al Biochim Biophys Acta Biomembr. 2019). It is also essentially undetected by SANS in a dilute aqueous solvent with 21% D2O, and offers the possibility to investigate deuterated membrane proteins structure and conformational changes in solution by SANS. We obtained for SpNox, a prokaryotic homolog of NADPH oxidase a first structural characterisation (Vermot et al Biophys J. 2020). We highlighted for the ABC (ATP-Binding Cassette) transporter BmrA, by combining SANS with X-ray crystallography, cryoEM, H/D exchange coupled with mass spectrometry and limited proteolysis, different conformational states during its ATPase cycle (Javed et al J Mol Biol. 2022). |
|---|
